Phaeodactylum tricornutum CCAP 1055/1 chromosome 28, whole genome shotgun sequence.
Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae; Phaeodactylum.
The Phaeodactylum genome reveals the evolutionary history of diatom genomes
Submitted (15-JUN-2017) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA
Submitted (12-AUG-2008) US DOE Joint Genome Institute, 2800 Mitchell Drive B100, Walnut Creek, CA 94598-1698, USA
PROVISIONAL REFSEQ: This record has not yet been subject to final\nNCBI review. The reference sequence is identical to CM000630.\nURL -- http://www.jgi.doe.gov/phaeodactylum\nJGI Project ID: 3634397\nContacts: Chris Bowler (cbowler@biologie.ens.fr)\n Igor Grigoriev (ivgrigoriev@lbl.gov)\nThe clone of P. tricornutum that was sequenced is CCAP1055/1 and is\navailable from the Culture collection of Algae and Protozoa\n(http://www.ccap.ac.uk). This clone represents a monoclonal culture\nderived from a fusiform cell in May 2003 from strain CCCP632, which\nwas originally isolated in 1956 off Blackpool (U.K.). It has been\nmaintained in culture continuously in F/2 medium.\nAnnotation was done by the JGI Annotation team and the Diatom\nConsortium.\nChromosomes 3 and 11 are complete and present in GenBank records\nCP001142 and CP001141, respectively.\nThe JGI and collaborators endorse the principles for the\ndistribution and use of large scale sequencing data adopted by the\nlarger genome sequencing community and urge users of this data to\nfollow them. It is our intention to publish the work of this\nproject in a timely fashion and we welcome collaborative\ninteraction on the project and analysis.\n(http://www.genome.gov/page.cfm?pageID=10506376)\nAnnotated scaffolds were added in December 2008.\n\n##Genome-Annotation-Data-START##\nAnnotation Provider :: INSDC submitter\nAnnotation Status :: Full annotation\nAnnotation Pipeline :: Eukaryotic Annotation Propagation Pipeline\n##Genome-Annotation-Data-END##
contains Tetratricopeptide-like helical domain; This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix, where the repeats that make up this structure are arranged about a common axis, These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids
probable Aspartate amino transferase aminoacid metabolism
Precise function unknown. Contains N-terminal targeting peptide and ankyrin domain proximal to C-terminus.; Ankyrin-repeat-containing gene of unknownn function
Homologous to the rpl14 gene in the chloroplast genome of C. reinhardtii
calnexin/calreticulin cycle-Endoplasmic Reticulum quality control
putative hydroxyacylglutathione hydrolase().Pyruvate metaboli
Probable hydroxyacylglutathione hydrolase Lactate metabolism
catalytic subunit participating with PCNA in DNA replication late in S phase
thiolase superfamily gene; acetoacetyl-coenzyme A thiolase
cytosolic glucose-6-phosphate isomerase, see also GenBank DQ812891, another GPI (Protein ID 53878, Phatr2/chr_28:197023-198828) is encoded directly downstream of this gene in reverse orientation
cytosolic glucose-6-phosphate isomerase, another GPI (Protein ID 23924, Phatr2/chr_28:194949-197014) is encoded directly downstream of this gene in reverse orientation
Transaldolase, involved in pentose-phosphate pathway, plastidic enzyme, possesses N-terminal bipartite targeting sequence
Formylmethionine deformylase probaly catalyzes N-formyl-L-methionine+H2O =formate+L-methionine.
The function of this gene is still unkown but the gene product is probably transported into the lumen of the plastid. Evidence by the presence of a signal peptide sequence at the 5'end of this gene. Cleavage site is VEA-FA. Another hydrophobic aa sequence is beginning behind the predicted cTP. Behind this second hydrophobic aa sequence is the typical cleavage site for the lumenal processing peptidase (AXA).
required for spermine/spermidine biosynthesis