ID B7FXN2_PHATC Unreviewed; 675 AA.
AC B7FXN2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEC48570.1};
GN ORFNames=PHATRDRAFT_45428 {ECO:0000313|EMBL:EEC48570.1};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC48570.1, ECO:0000313|Proteomes:UP000000759};
RN [1] {ECO:0000313|EMBL:EEC48570.1, ECO:0000313|Proteomes:UP000000759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC48570.1,
RC ECO:0000313|Proteomes:UP000000759};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
RN [2] {ECO:0000313|Proteomes:UP000000759}
RP GENOME REANNOTATION.
RC STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA Rokhsar D., Bowler C.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; CM000610; EEC48570.1; -; Genomic_DNA.
DR RefSeq; XP_002179584.1; XM_002179548.1.
DR AlphaFoldDB; B7FXN2; -.
DR STRING; 556484.B7FXN2; -.
DR PaxDb; 2850-Phatr45428; -.
DR EnsemblProtists; Phatr3_J45428.t1; Phatr3_J45428.p1; Phatr3_J45428.
DR GeneID; 7200675; -.
DR KEGG; pti:PHATRDRAFT_45428; -.
DR eggNOG; KOG1335; Eukaryota.
DR HOGENOM; CLU_407415_0_0_1; -.
DR InParanoid; B7FXN2; -.
DR OMA; CLRGRVF; -.
DR OrthoDB; 5486966at2759; -.
DR Proteomes; UP000000759; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000759};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..484
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 538..642
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 675 AA; 71808 MW; 1F614B2F7FD9DA6B CRC64;
MEVFGSVYLW TLASVVWLAV SVSLRYDPIR SDAYIQKERS SPHESTIHYL WERPLKRVRV
RNTNRSTHCY LSHVISMLSL SKTLLSPTLL LLISATSVVS FQAHHAIRTI ETRQRGTPAR
GVTSTALNDS SKPYDLAIVG AGVVGALAAV TAAQAPFHKR VILIDAPTAS GTLQSPSGQD
LSLGGPTGLF SKALRDTSKR IKVSTLRGMG LREDSVWNEI INSCVDLAAS NSEDIERQLD
MAGVTFLQGF AAFADSGGTD NLVVSQKDGS SSIVKAERVL LATGSQPFRP GGVPFDGKRV
FDSDSINGLS YLPKSVAITG SGIIAVEFAK IFRNLGADVT LIIRDQVPRN ALMKIGLDKD
VAATLVADLI RSGIHIERGA QAADFEVPTS SDRAPIRIAL EAKGGGPRAP GLRTELKCDA
YLAAVGRKPN TGNLNLNAAG IQVDEYGGVL VDSQLCTTAN AGNVYAAGDI LGRPFLASTG
VAQGKASITS MFGEMFKDSG KSVPQCEDGD TSCIVDGIAS AGISFDPASL ASNPFAFPTG
VWSSPEAAYY GLSTQQAKDM GIDADEGMAL YAECLRGRVF SPNGLLKIVF EKPAGRILGV
HICGDDACEL IHYGMELVKG RRTVLDLTDS LYSAVTFHEM YRIAAQAALD QAGARKRRAA
AGLALAKRNR QVVQK
//
