Phaeodactylum tricornutum CCAP 1055/1 chromosome 18, 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 CM000620.\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##
3R-hydroxyacyl-[acyl carrier protein] dehydrase
Subunit of fatty acid synthase. Dehydrates 3R-hydroxyacyl-[acyl carrier protein] intermediates to trans-2,3-enoyl-[acyl carrier protein] intermediates in saturated fatty acid biosynthesis. Probably plastid targetd via bipartite targeting sequence. TargetP only detects intitial secretory signal.
ligase activity, homolog to Phytophthora UBC
Phosphoglycerate/bisphosphoglycerate mutase
contains HMG1/2 (high mobility group) box, DNA-binding
putative oxidoreductase activity, electron transport
Kinesin-related motor protein required for mitotic spindle assembly and chromosome segregation
Catalyzes the formation of malonyl-CoA from acetyl-CoA and bicarbonate with the hydrolysis of ATP to ADP + P. Requires biotin as a co-factor. Represents the first committed enzyme of fatty acid biosynthesis.; biotin carboxylase
enzyme involved in N-glycan biosynthesis; Transfers an alpha-D-mannosyl residue from dolichyl-phosphate D-mannose into membrane lipid-linked oligosaccharide
synaptobrevin-domain containing protein, putative divergent v-SNARE component
Hypothetical protein, no alignments with known genes or protein domains, possible peroxidase-like domain, good EST support
A flavoprotein (FAD). Acts on primary amines, and usually also on some secondary and tertiary amines.
Member of Ca-ATPase family, high homology to sarcoplasmic-endoplasmic reticulum type (ATP2A-type). Good EST support.
glycolate oxidase (glycolate dehydrogenase), FMN-dependent alpha-hydroxy acid dehydrogenase; part of the photorespiratory pathway; contains peroxisomal targeting sequence (PTS1)
Sigma (small) subunit of the AP2 vesicle coat complex, ortholog of T. pseudonana TPS_154941
Glutaredoxin, probably plastidic, contains N-terminal bipartite plastid targeting presequence
glutathione peroxidase domain-containing protein
Hypothetical protein with glutathione peroxidase domain; glutathione peroxidases are involved in oxidative stress responses; they catalyze the reduction of hydroxyperoxides using glutathione: 2 Glutathione + H 2 O(2) = oxidised Glutathione + 2H 2 O
FEN-1 is a nuclease containing HhH2 and XPG motifs which cleaves between the RNA primer and the new DNA strand. Highly closed to Thalassiosira protein thaps1 132436
Caltractin (Centrin), Protein of the Calmoduline like superfamily (EF hand domain protein)
putative heme containing ferric reductase; contains DOMON domain, capable of catecholamine-binding; cell surface protein
bifunctional trehalose-6-phosphate synthase
Dual function enzyme which catalyzes the synthesis of trehalose. The two reactions catalyzed: (1) UDP-glucose + D-glucose 6-phosphate = UDP + trehalose 6-phosphate; and (2) trehalose 6-phosphate + H2O = trehalose + phosphate.; glycosyl transferase family 20
hypothetical protein with similarities to glyoxylate/hydroxypyruvate reductase (D-isomer-specific 2-hydroxy acid dehydrogenase superfamily)