ID A0A024T8S5_9STRA Unreviewed; 340 AA.
AC A0A024T8S5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Fatty acid desaturase domain-containing protein {ECO:0000259|Pfam:PF00487};
GN ORFNames=H310_14680 {ECO:0000313|EMBL:ETV90555.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV90555.1};
RN [1] {ECO:0000313|EMBL:ETV90555.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV90555.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KI914032; ETV90555.1; -; Genomic_DNA.
DR RefSeq; XP_008880805.1; XM_008882583.1.
DR AlphaFoldDB; A0A024T8S5; -.
DR STRING; 157072.A0A024T8S5; -.
DR EnsemblFungi; H310_14680-t26_1; H310_14680-t26_1-p1; H310_14680.
DR EnsemblProtists; ETV90555; ETV90555; H310_14680.
DR GeneID; 20091730; -.
DR VEuPathDB; FungiDB:H310_14680; -.
DR eggNOG; KOG1600; Eukaryota.
DR OrthoDB; 637961at2759; -.
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: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 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.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU000581};
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000581};
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 23..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..258
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 340 AA; 39051 MW; 97583DFB089D022A CRC64;
MTDGARAPVF GSPTPSFSWD EVVWYNVAIL SVWHAMALYT LFFVLPEASF LSIMTLWIGL
WFFSGLGITA GAHRLWAHRS YKARFPLQVF LALCNSMAFQ GSIFEWSRDH RVHHKGSDTT
ADPHNSRRGF FFAHMGWVMV RKHADVFREG KKMNFTDLEK DPLVQFQKKH YLASVLVMCY
AFPTLVGYLC FNSAWQGFWI GGVYRHVWVL HMTWCVNSVA HFFGYKPYDR NSRAVENLFV
SIGAIGEGWH NYHHRYPTDY ATGEMGVTGQ WNPTKGFIDI MACLGLAYDM KRSTTAAATR
EKNKIAVDQE ILKGVLQPPS SMDQFVNWLF FGRTEDQSVF
//
