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Database: UniProt
Entry: A0A1Q9C308_SYMMI
LinkDB: A0A1Q9C308_SYMMI
Original site: A0A1Q9C308_SYMMI 
ID   A0A1Q9C308_SYMMI        Unreviewed;       533 AA.
AC   A0A1Q9C308;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Delta-9 desaturase-like 2 protein {ECO:0000313|EMBL:OLP77303.1};
GN   ORFNames=AK812_SmicGene42649 {ECO:0000313|EMBL:OLP77303.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP77303.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLP77303.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP77303.1,
RC   ECO:0000313|Proteomes:UP000186817};
RA   Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA   Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA   Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT   "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT   adaptations to a symbiotic lifestyle.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00009295}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLP77303.1}.
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DR   EMBL; LSRX01001796; OLP77303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9C308; -.
DR   OrthoDB; 5487114at2759; -.
DR   Proteomes; UP000186817; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   InterPro; IPR015876; Acyl-CoA_DS.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR   PANTHER; PTHR11351:SF31; DESATURASE 1, ISOFORM A-RELATED; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          161..382
FT                   /note="Fatty acid desaturase"
FT                   /evidence="ECO:0000259|Pfam:PF00487"
FT   REGION          510..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  60742 MW;  0AE8AB42F382437F CRC64;
     MATYHWHLAG AVRALVYLVL LYQHWPSLNK LRWSTWPYEM TGRYAVGVFI VLIARYAGGG
     LAGLKKELHG LGKDAFGILA TVKVVYLSPV REVCSEAILK VCLLQDYVRY GPFGTVSGFM
     FQQPFAVGCQ LWAHFARRSE HFEPQLEDAE WWGIVSIEML LCALVFMIFF WMAVFAANVL
     HRYFSHRCFQ TSRLWSFALG AFSCMGSGMR PLQYSALHRR HHRFCDQEGD PHSPYQKGFF
     YAYVFCYADR DNLEIRPAFV RDWLLKNPEL LLLELYGGNV KALLRRKLLY TMVYALSPVW
     LQHFPLDVHP MTMAANLGEV LAINLVSAFN GFSHEIGWGV PDTDRCSHVN ACKGRDMPGF
     VMIGGGEAYH KEHHKFPNLA VYGHWYLDWS FCAYAAMEKC CLVWDLQRPP ATDNLIGIAE
     KFNWETTLRS PGRNRETDVR STWDARRQLE GLEERTASAV AYLHRQLLDL QAAQSPKTSS
     DVAVRLDALE QKQQQTAHRL DAVADVASSC SKEQDVRRTV PVSNAGAFNT QDS
//
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