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Database: UniProt
Entry: A0A1F8ACE2_9EURO
LinkDB: A0A1F8ACE2_9EURO
Original site: A0A1F8ACE2_9EURO 
ID   A0A1F8ACE2_9EURO        Unreviewed;       349 AA.
AC   A0A1F8ACE2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Elongation of fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU361115};
GN   ORFNames=ABOM_003529 {ECO:0000313|EMBL:OGM49416.1};
OS   Aspergillus bombycis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM49416.1, ECO:0000313|Proteomes:UP000179179};
RN   [1] {ECO:0000313|EMBL:OGM49416.1, ECO:0000313|Proteomes:UP000179179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX   PubMed=27664179;
RA   Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT   "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT   bombycis.";
RL   Genome Biol. Evol. 0:0-0(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC         chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC         EC=2.3.1.199; Evidence={ECO:0000256|ARBA:ARBA00001906};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + H(+) + malonyl-CoA = a 3-oxoacyl-CoA + CO2 +
CC         CoA; Xref=Rhea:RHEA:50252, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:90726; Evidence={ECO:0000256|RuleBase:RU361115};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50253;
CC         Evidence={ECO:0000256|RuleBase:RU361115};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ELO family. {ECO:0000256|RuleBase:RU361115}.
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:OGM49416.1}.
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DR   EMBL; LYCR01000009; OGM49416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8ACE2; -.
DR   STRING; 109264.A0A1F8ACE2; -.
DR   OrthoDB; 2312411at2759; -.
DR   Proteomes; UP000179179; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR030457; ELO_CS.
DR   InterPro; IPR002076; ELO_fam.
DR   PANTHER; PTHR11157:SF134; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 6; 1.
DR   PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01151; ELO; 1.
DR   PROSITE; PS01188; ELO; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW   ECO:0000256|RuleBase:RU361115};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW   ECO:0000256|RuleBase:RU361115};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361115};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361115};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361115};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361115};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361115};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361115}.
FT   TRANSMEM        56..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        86..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        227..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        265..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   REGION          318..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   349 AA;  39680 MW;  0633BFD0CE3CF0FD CRC64;
     MALEFLQNVP RPTIDRPFGI HLWPIFDQAF EKVVGYPASE FKFVEGETPM SGFRETAAML
     VTYYIVIFGG RMVMKNFPAL KLNTLFMIHN FYLTAISATL LALFIEQLLP TIWRNGIFFA
     ICDYEGGWTQ PLIVLYYVST LNYLTKYLEL IDTVFLFLKK KPLTFLHTYH HGATALLCYT
     QLIGLTAVQW VPITINLLVH VVMYWYYFQS ARGIRIWWKE WITRLQIIQF VIDLGFVYFA
     SYTYFSSTYF PWAPNMGKCA GEEFAAFAGM AILSSYLFLF ISFYIATYNK AAKTGRPRRN
     TGRQAVIDMA KMEVVPSANG SAANGSAKSN GAATASGRSN GPVTRSRKA
//
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