ID A0A443RL54_9ACAR Unreviewed; 344 AA.
AC A0A443RL54;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Stearoyl-CoA desaturase-like protein {ECO:0000313|EMBL:RWS15997.1};
DE Flags: Fragment;
GN ORFNames=B4U79_05668 {ECO:0000313|EMBL:RWS15997.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS15997.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS15997.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS15997.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|RuleBase:RU000581};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000256|RuleBase:RU000581}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295, ECO:0000256|RuleBase:RU000581}.
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:RWS15997.1}.
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DR EMBL; NCKU01000322; RWS15997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443RL54; -.
DR STRING; 1965070.A0A443RL54; -.
DR Proteomes; UP000285301; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR PANTHER; PTHR11351:SF31; DESATURASE 1, ISOFORM A-RELATED; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU000581};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW Lipid metabolism {ECO:0000256|RuleBase:RU000581};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000581};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000581};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..291
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
FT NON_TER 344
FT /evidence="ECO:0000313|EMBL:RWS15997.1"
SQ SEQUENCE 344 AA; 41008 MW; C00CF5AEC1C4193C CRC64;
MAPTSANHLP RYYPMSEKSV VRYSNLEEQV SKELKWFYVR YMNNARYLYV DSNYYGIVWP
NLILFVVMHL FYFYGLYMVL RIWPVGGMVF CICYGEIAGL GVTTGAHRLW THRSYEATLP
LRIFLCMCHT MAGQNDLYTW VRDHRLHHKF SETDADPHNS LRGMFFAHVG WLLTRKHPDV
MIKGRTIDMS DVINDPVVRF QRRFYVPLYI FFRFFIPTYL PMRYMNATFS QAFIGLFGTY
LGSLHCTWFV NSLAHWWGTK EYNVKIKPRN NFFVSYITLG EGFHNFHHTF PWDYTIGEFV
WQFNPGQKFI EFWAKIGLAK NLKRATPEQV KNRLENARKI KDQN
//
