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Database: UniProt
Entry: A0DIU9_PARTE
LinkDB: A0DIU9_PARTE
Original site: A0DIU9_PARTE 
ID   A0DIU9_PARTE            Unreviewed;       621 AA.
AC   A0DIU9;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Chromosome undetermined scaffold_52, whole genome shotgun sequence {ECO:0000313|EMBL:CAK82966.1};
GN   ORFNames=GSPATT00017323001 {ECO:0000313|EMBL:CAK82966.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK82966.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK82966.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK82966.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00009295}.
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DR   EMBL; CT868452; CAK82966.1; -; Genomic_DNA.
DR   RefSeq; XP_001450363.1; XM_001450326.1.
DR   AlphaFoldDB; A0DIU9; -.
DR   STRING; 5888.A0DIU9; -.
DR   EnsemblProtists; CAK82966; CAK82966; GSPATT00017323001.
DR   GeneID; 5036148; -.
DR   KEGG; ptm:GSPATT00017323001; -.
DR   eggNOG; KOG4232; Eukaryota.
DR   HOGENOM; CLU_030320_1_0_1; -.
DR   InParanoid; A0DIU9; -.
DR   OMA; HHIHCND; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProt.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR012171; Fatty_acid_desaturase.
DR   PANTHER; PTHR19353:SF19; DELTA(5) FATTY ACID DESATURASE C-RELATED; 1.
DR   PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        333..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        364..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        428..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        467..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          198..274
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   621 AA;  73677 MW;  F848F4E3CF47AA1B CRC64;
     MGDLKISTLN LTKRYSNSFQ LFLMVHSHRV FRGFFIMLLL FHMILLLVPW IEIKIPAWPI
     LKIKFAIGTS LWPFPTIDML SEENLYLRQI LMKTLEISVI MLYAIDLLPK IFIWRQNVLW
     KFVNIVILSQ MMFLLPVSII AYDKFALPTD TMKLRIFSIS FCFVIVCEIL SIREQKSLRF
     LQINQRQQEK QRQIKQKTQE FSWCEIVKHD SPNDCWIVIK DKIYDVTQFL QYHPGGNMIL
     DGAGGDCTAL WYSYHPSNLT KQEPPQKYLI GKVRDHQQYY SYDDDFYQNI KEEVEQKIPR
     NKWQNHWILF VKGFLCLTGY LACLYYYINY CTLLSAILLG FLAAQADVNI MHDGNHYAFS
     SNKTISFLAG YVLDLTFSTS VVYRRSHNFG HHSCVNHLEL DRAFDTTFPY IRLHPLQQRF
     WYHKYQHLYI WIIYTFVNFT DVFGTFDEMQ WFSNFPCRRG YVSKLQVFLQ IIVKLLWISL
     TLIYPSIKFS YKVAFGMWFV YNAVHSYNYA LYFSVNHWTL EAGVVDNQNI NQTNWGKLQI
     QNSSNFAVDS FIWTHLSGGL NYQIEHHLFP QFAHTRLKEI KNTIQVKAKQ ANIKYFEFPS
     FLDALISHYR LLKILGSQDL I
//
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