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Database: UniProt
Entry: A0A3N4IKT9_ASCIM
LinkDB: A0A3N4IKT9_ASCIM
Original site: A0A3N4IKT9_ASCIM 
ID   A0A3N4IKT9_ASCIM        Unreviewed;       297 AA.
AC   A0A3N4IKT9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Elongation of fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU361115};
DE   Flags: Fragment;
GN   ORFNames=BJ508DRAFT_199404 {ECO:0000313|EMBL:RPA86489.1};
OS   Ascobolus immersus RN42.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Ascobolaceae; Ascobolus.
OX   NCBI_TaxID=1160509 {ECO:0000313|EMBL:RPA86489.1, ECO:0000313|Proteomes:UP000275078};
RN   [1] {ECO:0000313|EMBL:RPA86489.1, ECO:0000313|Proteomes:UP000275078}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN42 {ECO:0000313|EMBL:RPA86489.1,
RC   ECO:0000313|Proteomes:UP000275078};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(2018).
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}.
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DR   EMBL; ML119649; RPA86489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4IKT9; -.
DR   STRING; 1160509.A0A3N4IKT9; -.
DR   Proteomes; UP000275078; 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; IPR002076; ELO_fam.
DR   PANTHER; PTHR11157:SF126; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 4; 1.
DR   PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01151; 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|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU361115};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU361115};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361115};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275078};
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        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        69..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        221..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        256..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RPA86489.1"
FT   NON_TER         297
FT                   /evidence="ECO:0000313|EMBL:RPA86489.1"
SQ   SEQUENCE   297 AA;  33259 MW;  C3CE948D4093DBD2 CRC64;
     IQNFLAGPHP QTIPAAPYPA SPFSISPETY EWWLQPAIPL TIATVYATSA HLANHFANGK
     PYAIAKTRAF KLFVLLHNLF LAVYSAWTFV GMTRAVHRSI KWDRGLPGAV DDFCNIQGDG
     KLWSEGLAFY GWWFYLSKFY EVIDTMVILA KGKKSSTLQT YHHTGAMLCM WAGVKYMAGP
     IWIFCVFNSA IHTLMYTYYF ITAMRLPFPM FLKRSLTSLQ ITQFLVGGSA AASYLFIGLL
     PDGISKKHCL QTSGEVFAVI LNVAYLTPLT YLFVRFFVDS YTKKGNSAKT ATKNGAN
//
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