ID J3KAF8_COCIM Unreviewed; 672 AA.
AC J3KAF8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Elongation of fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU361115};
GN ORFNames=CIMG_03029 {ECO:0000313|EMBL:EAS32005.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS32005.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704916; EAS32005.3; -; Genomic_DNA.
DR RefSeq; XP_001243588.2; XM_001243587.2.
DR AlphaFoldDB; J3KAF8; -.
DR STRING; 246410.J3KAF8; -.
DR GeneID; 4563815; -.
DR KEGG; cim:CIMG_03029; -.
DR VEuPathDB; FungiDB:CIMG_03029; -.
DR InParanoid; J3KAF8; -.
DR OMA; WNQGLAY; -.
DR OrthoDB; 2312411at2759; -.
DR Proteomes; UP000001261; 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:UP000001261};
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 62..79
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 231..254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 407..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT REGION 554..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 73309 MW; 837A5B98373ABE51 CRC64;
MGLFRSTERP DLPSVHLGLP PRSLLRFPPG SQPGTIPAPP VERSWLQPFT IPPKLYNDAL
KVQVPITIAL VYATTVILLN RINKKRGNRP WAISKTKPFH LFVVLHNVFL AVYSAWTFLG
MLDAFRESWP ARSEMHGSGL VNVVDAFCKI NGPRGLGNAA VYDTDAGSWT IFNPEYKLGP
GNVPDPTDVG RLWNKGLAFF GWIFYLSKFY EVLDTAIILA KGKKSSTLQT YHHAGAMMCM
WAGIRFMAAP IWIFALVNSA IHALMYTYYT LTALSVRIPV RIKKSLTTMQ ILQFIFGTSL
AASHLFIYYS IPFPVPHAVA LRPLASVMPS VAGAANESQA GVGSWLKKLA LRAAGHEGVA
ENIVNSNGTL FGPDGMQAAQ AALGKQEIRY ALQSRTFTCM DTSGQGFAIW LNVFYLLPLT
WLFARFFIRS YLRRTETAAK RSLTDSLAAE KAGLDALKGV TREIQNAVIE MHGDGNGTTD
NESGASTPQH PEAYEANVEN IMSARQARAE RRYSATTKHP VGISLAKGDS AGTRTPMDPA
AYGANIEDIM TRKQQGVEEK AHRVAKHPEP PHLSRSSKEG IRTPLNERGY EANLEDVMSP
AQRKLGGRQP SSEPKEKTME APWVPVRGSK AGNKKGTKAG GKTGASSSLS LSSSPTKGSG
FKVLADEHVG TA
//
